Peroxisome proliferator-activated receptor γ activators affect the maturation of human monocyte-derived dendritic cells

Gosset, Philippe; Charbonnier, Anne-Sophie; Delerive, Philippe; Fontaine, Josette; Staels, Bart; Pestel, Joël; Tonnel, André‐Bernard; Trottein, François

doi:10.1002/1521-4141(2001010)31:10<2857::aid-immu2857>3.0.co;2-x

Cited by 206 publications

(189 citation statements)

References 42 publications

(53 reference statements)

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Section: Discussionmentioning

confidence: 99%

“…The mechanism by which oxidized LDL or linoleic acid metabolites up-regulate CD36 involves activation of the transcription factor PPARc [13,35]. Other PPARc ligands such as 15d-PGJ2 and the thiazolidinedione class of anti-diabetic drugs also increase CD36 expression notably in Mu [13] but also in mature and immature human monocyte-derived dendritic cells [36].The CD36 promoter contains a PPARc-9-cis-retinoic acid receptor binding site, and the PPARc-9-cis-retinoic acid receptor complex can modulate CD36 gene expression through direct promoter interaction [35].Several authors report that scavenger receptors can cooperate with Toll-like receptors (TLR) in microbial sensing, enhancing inflammatory signals [37]. In particular, it has been shown recently that several components of Gram-positive bacteria such as lipoteichoic acid can form TLR2/6 heterodimers with CD36 [38].…”

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confidence: 99%

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IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

et al. 2007

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The class B scavenger receptor CD36 is a component of the pattern recognition receptors on monocytes that recognizes a variety of molecules. CD36 expression in monocytes depends on exposure to soluble mediators. We demonstrate here that CD36 expression is induced in human monocytes following exposure to IL-13, a Th2 cytokine, via the peroxisome proliferator-activated receptor (PPAR)c pathway. Induction of CD36 protein was paralleled by an increase in CD36 mRNA. The PPARc pathway was demonstrated using transfection of a PPARc expression plasmid into the murine macrophage cell line RAW264.7, expressing very low levels of PPARc, and in peritoneal macrophages from PPARc-conditional null mice. We also show that CD36 induction by IL-13 via PPARc is dependent on phospholipase A2 activation and that IL-13 induces the production of endogenous 15-deoxy-D 12,14 -prostaglandin J 2 , an endogenous PPARc ligand, and its nuclear localization in human monocytes. Finally, we demonstrate that CD36 and PPARc are involved in IL-13-mediated phagocytosis of Plasmodium falciparum-parasitized erythrocytes. These results reveal a novel role for PPARc in the alternative activation of monocytes by IL-13, suggesting that endogenous PPARc ligands, produced by phospholipase A2 activation, could contribute to the biochemical and cellular functions of CD36.Leukocyte signaling * These 2 authors contributed equally to this work. IntroductionThe innate immune system protects the host in the early phase of infection. Circulating monocytes and tissue macrophages (Mu) mediate much of this innate immune response [1]. The strategy of recognition in the innate response is mediated by the coordinated action of pathogen-associated molecular patterns and pattern recognition receptors. Scavenger receptors and mannose receptor are important pattern recognition receptors in monocytes/Mu [2,3]. The modulation of the expression of these receptors may be critical in the role of these cells in antigen processing, scavenging, and host defence against pathogens. Several members of the scavenger receptor family, including Mu class A scavenger receptors and CD36, have been identified as receptors for modified lipoproteins on Mu, and their relevance to lipid uptake has been demonstrated in vitro and in vivo [4]. The scavenger receptor CD36, an 88-kDa integral membrane protein, is a class B scavenger receptor expressed on a wide variety of cells, in particular on monocytes and monocytederived Mu [5,6]. CD36 is known as a receptor for the uptake of oxidatively modified low-density lipoprotein (LDL) [7] and is also able to bind anionic phospholipid phosphatidylserine [8]. This scavenger receptor is implicated in the clearance of apoptotic cells [9]. Recently, McGilvray and colleagues [10] described a CD36-dependent nonopsonic phagocytosis of erythrocytes containing P. falciparum, by monocytes and culture-derived Mu, and a decrease in the parasiteinduced TNF secretion by monocytes/Mu. These processes were accentuated by CD36 up-regulation by peroxisome proliferator-acti...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

et al. 2007

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“…Previous studies demonstrated that PPARs are not only expressed in adipose tissue but also in macrophages (Jiang et al, 1998;Ricote et al, 1998), dendritic cells (Gosset et al, 2001), B cells (Setoguchi et al, 2001), and T cells . PPARs have been shown to play an important role in regulating inflammation mediated by nuclear factor-kappa B (NF-κB).…”

Section: Ppars and Inflammationmentioning

confidence: 99%

The Nuclear Receptor PPARs as Important Regulators of T-Cell Functions and Autoimmune Diseases

Choi¹,

Bothwell

2012

Molecules and Cells

140

106

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Members of the nuclear receptor superfamily function as transcription factors involved in innate and adaptive immunity as well as lipid metabolism. These highly conserved proteins participate in ligand-dependent or -independent regulatory mechanisms that affect gene expression. Peroxisome proliferator-activated receptors (PPARs), which include PPARα, PPARβ/δ, and PPARγ, are a group of nuclear receptor proteins that play diverse roles in cellular differentiation, development, and metabolism. Each PPAR subfamily is activated by different endogenous and synthetic ligands. Recent studies using specific ligand treatments and cell type-specific PPAR knockout mice have revealed important roles for these proteins in T-cell-related autoimmune diseases. Moreover, PPARs have been shown to regulate T-cell survival, activation, and CD4 + T helper cell differentiation into the Th1, Th2, Th17, and Treg lineages. Here, we review the studies that provide insight into the important regulatory roles of PPARs in T-cell activation, survival, proliferation, differentiation, and autoimmune disease.

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“…Monocytes were then differentiated into DC by standard procedures [18]. Briefly, monocytes were cultivated at 10 6 cells/ml for 7 days in RPMI 1640 with 10% heatinactivated FCS (Invitrogen, Paisley, UK) containing 10 ng/ ml IL-4 and 25 ng/ml GM-CSF.…”

Section: Preparation Of Human Mddc and Naive T Cellsmentioning

confidence: 99%

“…Along with their action on DP, PGD 2 and/or PGD 2 metabolites can also act directly on intracellular targets. In particular, PGD 2 and 15-deoxy-d (12,14)PGJ 2 have been shown to activate peroxisome proliferator-activated receptor-c (PPAR-c) [17], a nuclear hormone receptor known to be expressed in human monocytes [18] and to affect many cellular functions, including DC differentiation [19] and maturation [18].…”

Section: Introductionmentioning

confidence: 99%

Prostaglandin D₂ affects the differentiation and functions of human dendritic cells: impact on the T cell response

et al. 2005

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The local environment in which dendritic cells (DC) differentiate is important for the acquisition of their immunostimulatory properties. Since prostaglandin D 2 (PGD 2 ), a major prostanoid produced during inflammatory reactions, is involved in the control of immune responses, its effect on the differentiation and functions of human monocytederived dendritic cells (MDDC) was studied. We show that DC differentiated in the presence of PGD 2 (PG/DC) have an unusual phenotype, with modifications in the expression of molecules involved in antigen (Ag) capture and presentation, leading to higher endocytic and Ag-processing activities. However, under conditions that necessitated Ag processing and presentation, PG/DC have an impaired ability to stimulate naive T cells, whereas superAg-pulsed DC efficiently promote their proliferation. Upon lipopolysaccharide or TNF-a/IL-1b stimulation, PG/DC phenotypically mature but produce abnormal amounts of immunoregulatory cytokines (decreased IL-12p70/IL-10 ratio). Moreover, mature PG/DC fail to up-regulate the chemokine receptor CCR7 and show an impaired migration towards its ligand CCL19. Finally, PG/DC favor the differentiation of naive T cells toward Th2 cells, an effect dependent on IL-10 and inducible costimulator ligand expression by DC. Most of the herein described effects of PGD 2 on MDDC can be reproduced, usually with a higher efficacy, with a selective D prostanoid receptor (DP)1, but not DP2, agonist. Taken as a whole, these results demonstrate that PGD 2 impacts DC differentiation and functions, and extend the concept that it exerts important roles in immunity.

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Peroxisome proliferator-activated receptor γ activators affect the maturation of human monocyte-derived dendritic cells

Cited by 206 publications

References 42 publications

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

The Nuclear Receptor PPARs as Important Regulators of T-Cell Functions and Autoimmune Diseases

Prostaglandin D₂ affects the differentiation and functions of human dendritic cells: impact on the T cell response

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Peroxisome proliferator-activated receptor γ activators affect the maturation of human monocyte-derived dendritic cells

Cited by 206 publications

References 42 publications

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

The Nuclear Receptor PPARs as Important Regulators of T-Cell Functions and Autoimmune Diseases

Prostaglandin D2 affects the differentiation and functions of human dendritic cells: impact on the T cell response

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Prostaglandin D₂ affects the differentiation and functions of human dendritic cells: impact on the T cell response